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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Receptor Downregulation in MVBs01:15

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Regulation of the Unfolded Protein Response

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Regulation of Bacterial Virulence

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A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
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Immune regulation by phospholipase C-β isoforms.

Wenbin Xiao1, Yuko Kawakami, Toshiaki Kawakami

  • 1Department of Pathology, University Hospital Case Medical Center, Case Western Reserve University, Cleveland, OH 44106, USA. wenbin.xiao@UHhospitals.org

Immunologic Research
|May 29, 2012
PubMed
Summary

Phospholipase C (PLC)-β plays a key role in cellular signaling, interacting with G protein-coupled receptors and functioning in the nucleus. This enzyme is crucial for immune cell activation and differentiation, and its dysregulation is linked to tumorigenesis.

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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Immunology

Background:

  • Recent advancements illuminate the functions of phospholipase C (PLC)-β, particularly its downstream signaling from G protein-coupled receptors and its nuclear activities.
  • PLC-β interacts with tyrosine kinase pathways, inhibiting Stat5 activation via SHP-1 recruitment.
  • A novel multimolecular signaling platform, the SPS complex, has been identified, implicating it in tumorigenesis and immune cell regulation.

Purpose of the Study:

  • To elucidate the multifaceted roles of PLC-β in cellular signaling and immune system modulation.
  • To investigate the involvement of PLC-β in the newly identified SPS complex.
  • To understand PLC-β's contribution to immune cell differentiation and activation.

Main Methods:

  • Investigating signaling pathways involving G protein-coupled receptors and tyrosine kinases.
  • Characterizing the molecular composition and function of the SPS complex.
  • Analyzing the impact of PLC-β on immune cell differentiation and activation.

Main Results:

  • Established PLC-β's function downstream of G protein-coupled receptors and in the nucleus.
  • Demonstrated PLC-β's inhibitory role in Stat5 activation through SHP-1 recruitment within the SPS complex.
  • Highlighted the regulatory significance of the SPS complex in tumorigenesis and immune responses.

Conclusions:

  • PLC-β is a critical signaling molecule with diverse roles in both nuclear and cytoplasmic functions.
  • The SPS complex represents a key platform for regulating tumorigenesis and immune cell activity.
  • PLC-β significantly contributes to the differentiation and activation of innate and adaptive immune cells.